Glyceraldehyde-3-phosphate dehydrogenase regulates cyclooxygenase-2 expression by targeting mRNA stability

被引：25
|
作者：
Ikeda, Yuki [1 ]
Yamaji, Ryoichi [2 ]
Irie, Kazuhiro [1 ]
Kioka, Noriyuki [3 ]
Murakami, Akira [1 ]
机构：
[1] Kyoto Univ, Grad Sch Agr, Div Food Sci & Biotechnol, Kyoto, Japan
[2] Osaka Prefecture Univ, Grad Sch Life & Environm Sci, Div Appl Biol Chem, Osaka, Japan
[3] Kyoto Univ, Grad Sch Agr, Div Appl Life Sci, Kyoto, Japan
来源：
ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS | 2012年 / 528卷 / 02期
基金：
日本学术振兴会;
关键词：
GAPDH; Cyclooxygenase-2; Post-transcriptional regulation; mRNA stability; Glutathione; Aggregation; POSTTRANSCRIPTIONAL REGULATION; FUNCTIONAL DIVERSITY; CANCER CELLS; PROTEIN; HUR; RECEPTOR; BINDING; GLUTATHIONE; MECHANISM; REGION;
D O I：
10.1016/j.abb.2012.09.004
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
Cyclooxygenase (COX)-2 is an inducible inflammatory protein whose expression is partially regulated at the post-transcriptional level. We investigated whether glyceraldehyde-3-phosphate dehydrogenase (GAPDH) binds to the AU-rich element (ARE) of COX-2 mRNA for its degradation. Knockdown of GAPDH in hepa1c1c7 cells significantly enhanced COX-2 expressions. Recombinant GAPDH bound to the COX-2 ARE within the first 60 nucleotides of the 3'-UTR via the NAD(+) binding domain. Interestingly, a C151S GAPDH mutant retained binding activity. Confocal microscopy observation revealed that LPS exposure reduced the localization of GAPDH in nuclei. Our results indicate that GAPDH negatively regulates COX-2 by binding to its ARE. (C) 2012 Elsevier Inc. All rights reserved.
引用
收藏
页码：141 / 147
页数：7
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